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InterPro: IPR008964 Invasin/intimin cell-adhesion

Protein matchesHelp
UniProtKB
Matches:
2075 proteins
AccessionHelp IPR008964 Invasin/intimin_cell_adhesion
TypeHelp Domain
SignaturesHelp
InterPro RelationshipsHelp
Found in IPR003535 Intimin bacterial adhesion mediator protein
Contains IPR003343 Bacterial Ig-like, group 2
IPR003344 Bacterial Ig-like, group 1
IPR015217 Invasin, domain 3
InterPro annotation
BioMart Logo Entry Details in BioMart
AbstractHelp

Two types of pathogenic Escherichia coli, enteropathogenic E. coli (EPEC) and enterohemorrhagic E. coli (EHEC), cause diarrhoeal disease by disrupting the intestinal environment through the intimate attachment of the bacteria to the intestinal epithelium. This process is mediated by intimin, an outer membrane protein that is homologous to the invasins of pathogenic Yersinia. EPEC and EHEC form characteristic lesions on infected mammalian cells called actin pedestals. Each of these two pathogens injects its own translocated intimin receptor (Tir) molecule into the plasma membranes of host cells. Interaction of translocated Tir with the bacterial outer membrane protein intimin is required to trigger the assembly of actin into focused pedestals beneath bound bacteria [1].

Structural linksHelp
SCOP: b.1.14.1

Taxonomic coverageHelp

Overlapping InterPro entriesHelp
IPR008964 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
P11922 Invasin

P19728 Minor capsid protein 10B

P32325 Protein DBF4

Q5VU65 Nuclear pore membrane glycoprotein 210-like

Q9D2F7 Nuclear pore membrane glycoprotein 210-like

More proteins


Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR015217 Invasin, domain 3
IPR003535 Intimin bacterial adhesion mediator protein
IPR016187 C-type lectin fold
IPR016186 C-type lectin-like
IPR006572 Zinc finger, DBF-type
IPR008964 Invasin/intimin cell-adhesion
IPR013117 Intimin, C-terminal
IPR003343 Bacterial Ig-like, group 2
IPR003344 Bacterial Ig-like, group 1
IPR013939 Regulatory subunit Dfp1/Him1, central region
PDB Chain
ModBase
CATH Domain
SWISS-MODEL
SCOP Domain

PublicationsHelp
1. Campellone KG, Leong JM.
Tails of two Tirs: actin pedestal formation by enteropathogenic E. coli and enterohemorrhagic E. coli O157:H7.
Curr. Opin. Microbiol. 6 82-90 2003 [PubMed: 12615225]
http://dx.doi.org/10.1016/S1369-5274(03)00005-5

Additional ReadingHelp
Hamburger ZA, Brown MS, Isberg RR, Bjorkman PJ.
Crystal structure of invasin: a bacterial integrin-binding protein.
Science 286 1999 291-5 [PubMed: 10514372]
http://dx.doi.org/10.1126/science.286.5438.291
Luo Y, Frey EA, Pfuetzner RA, Creagh AL, Knoechel DG, Haynes CA, Finlay BB, Strynadka NC.
Crystal structure of enteropathogenic Escherichia coli intimin-receptor complex.
Nature 405 2000 1073-7 [PubMed: 10890451]
http://dx.doi.org/10.1038/35016618
Batchelor M, Prasannan S, Daniell S, Reece S, Connerton I, Bloomberg G, Dougan G, Frankel G, Matthews S.
Structural basis for recognition of the translocated intimin receptor (Tir) by intimin from enteropathogenic Escherichia coli.
EMBO J. 19 2000 2452-64 [PubMed: 10835344]
http://dx.doi.org/10.1093/emboj/19.11.2452
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InterPro 23.1